EP2231205B1 - Pansement à base de collagène colloïdal pour blessures par brûlure produit à partir de méduse - Google Patents

Pansement à base de collagène colloïdal pour blessures par brûlure produit à partir de méduse Download PDF

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Publication number
EP2231205B1
EP2231205B1 EP09702854.2A EP09702854A EP2231205B1 EP 2231205 B1 EP2231205 B1 EP 2231205B1 EP 09702854 A EP09702854 A EP 09702854A EP 2231205 B1 EP2231205 B1 EP 2231205B1
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EP
European Patent Office
Prior art keywords
collagen
film
jellyfish
wound dressing
tissue
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Not-in-force
Application number
EP09702854.2A
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German (de)
English (en)
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EP2231205A4 (fr
EP2231205A2 (fr
Inventor
Samuel Angel
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Coll Med Ltd
Coll-Med Ltd
Original Assignee
Coll Med Ltd
Coll-Med Ltd
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Publication date
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Publication of EP2231205A2 publication Critical patent/EP2231205A2/fr
Publication of EP2231205A4 publication Critical patent/EP2231205A4/fr
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Publication of EP2231205B1 publication Critical patent/EP2231205B1/fr
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    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
    • A61K35/56—Materials from animals other than mammals
    • A61K35/614—Cnidaria, e.g. sea anemones, corals, coral animals or jellyfish
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
    • A61L15/00—Chemical aspects of, or use of materials for, bandages, dressings or absorbent pads
    • A61L15/16—Bandages, dressings or absorbent pads for physiological fluids such as urine or blood, e.g. sanitary towels, tampons
    • A61L15/42—Use of materials characterised by their function or physical properties
    • A61L15/44—Medicaments
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/39—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin, cold insoluble globulin [CIG]
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
    • A61L15/00—Chemical aspects of, or use of materials for, bandages, dressings or absorbent pads
    • A61L15/16—Bandages, dressings or absorbent pads for physiological fluids such as urine or blood, e.g. sanitary towels, tampons
    • A61L15/22—Bandages, dressings or absorbent pads for physiological fluids such as urine or blood, e.g. sanitary towels, tampons containing macromolecular materials
    • A61L15/32—Proteins, polypeptides; Degradation products or derivatives thereof, e.g. albumin, collagen, fibrin, gelatin
    • A61L15/325—Collagen
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
    • A61L15/00—Chemical aspects of, or use of materials for, bandages, dressings or absorbent pads
    • A61L15/16—Bandages, dressings or absorbent pads for physiological fluids such as urine or blood, e.g. sanitary towels, tampons
    • A61L15/40—Bandages, dressings or absorbent pads for physiological fluids such as urine or blood, e.g. sanitary towels, tampons containing ingredients of undetermined constitution or reaction products thereof, e.g. plant or animal extracts
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
    • A61L15/00—Chemical aspects of, or use of materials for, bandages, dressings or absorbent pads
    • A61L15/16—Bandages, dressings or absorbent pads for physiological fluids such as urine or blood, e.g. sanitary towels, tampons
    • A61L15/42—Use of materials characterised by their function or physical properties
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P17/00—Drugs for dermatological disorders
    • A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like

Definitions

  • the present invention is directed to burn wound dressings comprised of colloidal collagen gel produced from jellyfish.
  • the present invention is directed to films and film/fabric composites and methods for preparation thereof, wherein the films or film/fabric composites are produced from jellyfish and are comprised of a colloidal collagen salt with sufficient viscosity to enable production of a stable gel for use as a burn wound dressing film, without the need for outside cross-linking agents.
  • Collagen is used worldwide in cosmetics and pharmaceuticals. It is usually obtained from cattle hides, pork skins, or connective tissues from various animals, and it is usually extracted as soluble collagen. Collagen sources from animals carry with them the possibilities of infection with viral diseases such as BSE or Mad Cow Disease, Hoof and Mouth Disease, Hog Cholera, Avian Flu and others. The fastidious dehairing, blood and fat removal necessary from the skins of these animals also exposes the workers to infection from these above mentioned diseases, and results in relatively high costs.
  • viral diseases such as BSE or Mad Cow Disease, Hoof and Mouth Disease, Hog Cholera, Avian Flu and others.
  • the fastidious dehairing, blood and fat removal necessary from the skins of these animals also exposes the workers to infection from these above mentioned diseases, and results in relatively high costs.
  • Jellyfish blooms are increasing world wide and are thus becoming more and more of a nuisance and the cause of serious damage to the fishing industry.
  • An object of the present invention is to help transfer a nuisance or potential source of damage into a useful and beneficial commodity.
  • Jellyfish are comprised of approximately 97-98 % water and about 3% salt. Protein makes up most of the rest of the solids and the major part of that protein is collagen.
  • Collagen prepared from jellyfish is not subject to infection from animal diseases. Jellyfish are relatively easy to clean, and do not require dehairing, blood or fat removal, as in animal skins, nor do they depend on animal or fish skin removal and de-lipidation.
  • Collagen formation is an essential part of various phases of the healing process in serious 2 nd , 3 rd and 4 th degree burn wounds and wounds in general. Collagen is laid down in the human body and in tissue renewal in wounds by fibroblasts. The quicker and more effectively fibroblasts proliferate, the quicker collagen regenerative tissue can develop. Fibroblast proliferation is enhanced by adhesion to collagen scaffolds, particularly scaffolds including Types I, II, and/or III collagen. Collagen scaffolds constructed from jellyfish have shown superior human fibroblast cell proliferation and viability as compared to bovine collagen scaffolds (Collagen scaffolds derived from marine sources and their biocompatibility, Eun Song, So Yeon Kim et al. Biomaterials 27:29512961 2006 ).
  • collagen films for wound healing comprised from jellyfish collagen.
  • collagen films from jellyfish tissue have only been produced using solubilized collagen gels, which are generally not stable and turn rubbery upon standing. They are also not thermally stable without the introduction of cross-linking agents, which can potentially have adverse effects for wound dressing applications. It is an object of the present invention to produce collagen films for wound healing from non-solubilized jellyfish collagen, which would not require introduction of cross-linking agents.
  • US 6541023 is directed to the use of fish skin to obtain collagen for the production of supports for tissue engineering.
  • WO 99/63964 is directed to a method for preparing fibrillin from cnidaria.
  • a method of producing a collagen-based wound dressing includes providing a jellyfish tissue, adding an acid to the jellyfish tissue to produce a collagen-salt solution, mixing the collagen-salt solution to form a viscous gel, and forming a burn dressing from the viscous gel.
  • the wound dressing may be a film or a film/fabric composite.
  • the present invention relates to a collagen film or film/fabric composite made from a collagen-salt gel, and methods of preparation thereof
  • a collagen film is formed from a gel or slurry of a colloidal form of collagen extracted from jellyfish tissue.
  • bovine tissue is much more aqueous than animal or fish skins.
  • the solidity of bovine tissue allows for it to be freeze-dried and directly solubilized in acid.
  • the jellyfish tissue is highly aqueous, which makes the process of freeze-drying very time consuming and therefore expensive.
  • types of jellyfish such as the Rhopilema nomadica jellyfish tissue used in the examples of the present application, are comprised primarily of types II and III collagen, whereas bovine tissue is comprised mostly of type I collagen.
  • Type I collagen is more thermally stable than types II and III due to differences in amino acid composition, side chain composition, hydrophobic areas, etc. As such, the parameters for forming colloidal collagen from jellyfish must accommodate the relative thermal instability of the form of collagen found therein.
  • a jellyfish is provided (step 102).
  • the jellyfish is a Rhopilema nomadica jellyfish, commonly found along the coast of Israel.
  • the Rhopilema nomadica jellyfish has an umbrella made up of two cellular layers: the ectoderm and the endoderm. Between these two layers lies the mesoglea, a noncellular tissue with collagen fibers in a gelatinous substance. All three layers are used in the present invention, although embodiments of the invention may include use of only the mesoglea layer.
  • the jellyfish is any other type of jellyfish which may be suitable for formation of collagen films.
  • the jellyfish is cleaned (step 104) by removing tentacles and washing to remove sand and mucous membranes from the umbrella's endoderm.
  • the cleaned jellyfish tissue is cut into pieces and immediately frozen (step 106) and stored, for example, in shallow containers for rapid freezing so as to avoid deterioration of the collagen in the jellyfish tissue.
  • an amount of frozen jellyfish tissue is defrosted, and the defrosted water content is removed (step 108) from the remaining "solid material".
  • solid material refers to the remaining block of tissue after defrosted water has been removed. However, a large volume of the "solid material" is generally comprised of water as well.
  • the jellyfish tissue is frozen into blocks, a desired amount of frozen jellyfish tissue may be defrosted as needed. Removal of the defrosted water results in removal of some of the salt which is naturally present in the jellyfish tissue.
  • the remaining solid material is then rinsed (step 110) in deionized ice water to remove the excess salt. Rinsing may be done several times in a high volume of water (1:10 ratio of solid material volume to water volume, for example) to ensure that the salt is sufficiently removed.
  • the amount or concentration of starting fresh or frozen tissue used is approximately three times the amount as compared to cowhide for a similar yield of usable collagen gel. Generally, following desalting about 0.1% of the wet weight of the raw material will remain as dry weight. Of this, the collagen yield is approximately 90%.
  • the desalted, rinsed tissue is finely chopped (step 111), using, for example, a refrigerated bowl chopper maintained at approximately 0° C. Chopping may result in a paste-like consistency.
  • the chopped material is put into a container or vessel, which may include a magnetic stirrer or an overhead stirring mechanism.
  • An acid is added (step 112) in an amount to reach a predetermined acid concentration (which depends on the amount of water left in the material).
  • the pre-determined acid concentration and normality will depend on the isoelectric point of the tissue, which is determined (step 113) per batch as described above.
  • the amount of tissue in any given batch may vary depending on the availability of the particular jellyfish being used, but may be hundreds of kilograms worth or even more.
  • This determination may be done well in advance of the step of adding an acid to form the colloidal collagen salt. It is known that if the pH of a protein is below but near the isoelectric point, the more acid added, the more non inorganic protein is transformed into a salt. Thus the object is to maximize as much as possible this transformation to a protein salt colloid and to obtain maximum viscosity without causing a depressing effect by an excess of acid. In this way, a protein salt obtainable by stoichiometric combination of the acid with the jellyfish solids may be maximized. With hydrochloric acid the amount added is adjusted to between a normality of between 0.001 and 0.1 depending on the isoelectric point of the jellyfish tissue, and with jellyfish tissue at a calculated dry solids content at a concentration between 1 and 3%,.
  • the collagen-salt solution is mixed, by stirring, blending or agitation, (step 114) to form a viscous gel. In one embodiment, this is done by grinding and forming a homogenate. In another embodiment, stirring may be done using a magnetic stirrer. Blending may be accomplished by using a blender type apparatus to sufficiently stir the acid with the chopped material. The use of more aggressive agitation using a blender may be required to obtain maximum protein salt formation.
  • the rate of stirring may be in a range of 1,000-10,000 rpm, for example, but is not limited to those speeds.
  • the temperature is adjusted to 0 centigrade and the entire apparatus is placed under vacuum.
  • Slow agitation commences for about 10 minutes to allow thorough mixing of the acid with the umbrella tissue.
  • Agitation is then increased and can reach 10,000 rpm.
  • Temperature is monitored not to surpass 25 degrees centigrade during the mixing-blending operations.
  • Agitation and blending can take between 10 to 30 minutes to obtain the optimum viscosity required for a film formation with desirable tensile strength properties.
  • the viscosity of the gel and the thermal stability will vary based on jellyfish tissue concentration, acid pH, agitation speed, agitation time and other parameters. Thermal resistance to denaturation may be tested at different temperatures.
  • Viscosity measurements may be taken using any standard viscometer at various intervals, for example.
  • a free-standing film 300 is formed as follows. First, measured amounts of the viscous liquid are poured into film molds and dried under vacuum in a vacuum oven at a relatively low temperature (approximately 20°-30° C) to create a film. Once the film is dried, the temperature may be raised to 100°-110° C and heated for a period of time (approximately 24 hours) under vacuum.
  • This last step can simultaneously enhance the natural cross-linking of the collagen, providing greater stability, while also sterilizing the film. If done for too long or at too high a temperature, the collagen may start to denature. In other embodiments, the viscous liquid may be directly formed into a film using adapted sheeting methods. In some embodiments, following film formation, the films or samples of the films may be tested (step 118) for fibroblast proliferation.
  • Films may vary in thickness from 25 to 100 microns. The more spread out the gel is, the thinner the film will be. In some embodiments, small amounts of food grade agents may be added to enhance film pliability and/or stability. In addition, any enhancement agents, such as vitamin C or other natural healing elements may be added. Films may be tested for fibroblast attachment and proliferation in vitro, and may be used for wound dressings and other applications.
  • a film/fabric composite 400 is formed either by immersing a piece of fabric 404 in the gel, or by injecting the viscous colloid liquid via an injection device 402 such as syringe into the piece of fabric 404.
  • Fabric 404 may be gauze, woven fabric, or any other suitable fabric.
  • fabric 404 is comprised of structural elements 406 and pores 408.
  • Structural elements 406 may have a rope-like structure, a weave-like structure, or any other structure which may allow for the presence of pores 408.
  • the film/fabric composite may be dried under vacuum in a vacuum oven at a relatively low temperature (approximately 20°-30° C). Once the film is dried, the temperature may be raised to 100°-110° C and heated for a period of time (approximately 24 hours) under vacuum.
  • An advantage of this embodiment is that pores are naturally present in the material, which can enhance exudation and healing of the wound.
  • it may be necessary to introduce pores which can be done, for example, by deaerating and then injecting air into the gel at a fixed rate and speed, or by using lasers.
  • small amounts of food grade agents may be added to enhance film pliability and/or stability.
  • any enhancement agents such as vitamin C or other natural healing elements may be added.
  • Film/fabric composites may be tested for fibroblast attachment and proliferation in vitro, and may be used for wound dressings and other applications.

Claims (15)

  1. Procédé de fabrication d'un gel à base de collagène, le procédé comprenant les phases suivantes:
    fourniture d'un tissu de méduse ;
    désalinisation dudit tissu de méduse ;
    hâchage dudit tissu de méduse ;
    détermination d'un point isoélectrique dudit tissu de méduse ;
    addition d'un acide ayant une concentration et une molarité liées à un point isoélectrique dudit tissu de méduse, audit tissu de méduse pour produire un colloïde de sel collagène; et
    mélange dudit colloïde de sel collagène pour constituer un gel visqueux.
  2. Procédé selon la revendication 1, consistant en outre à former un film ou bien un composite de film et de tissu à partir dudit gel.
  3. Procédé selon la revendication 1, où ladite addition d'un acide consiste à ajouter un fort acide avec une concentration dans une plage comprise entre 0,001 et 0,1 M pour une solution à 1-3 % de tissu de méduse.
  4. Procédé selon la revendication 1, consistant en outre à surveiller un pH pendant ladite addition d'un acide.
  5. Procédé selon la revendication 1, où ledit mélange comprend au moins l'une des opérations suivantes : homogénéisation, brassage, malaxage, agitation ou toute combinaison de ceux-ci.
  6. Procédé selon la revendication 1, où l'on effectue des mesures de viscosité pendant ledit mélange.
  7. Procédé selon la revendication 2, consistant en outre à sécher le film pendant un laps de temps donné sous air déshumidifié ou sous vide, de préférence lorsque ledit séchage consiste en outre à stériliser le film.
  8. Procédé selon la revendication 2, consistant en outre à rechercher la prolifération des fibroblastes dans le film ainsi obtenu.
  9. Procédé selon l'une quelconque des revendications précédentes, consistant en outre à former un pansement à partir dudit gel.
  10. Pansement comprenant : un gel à base de collagène colloïdal que l'on peut obtenir avec le procédé de la revendication 9 à partir de tissu de méduse configuré pour être appliqué sur une blessure.
  11. Pansement de la revendication 10, où ledit gel à base de collagène colloïdal est un film ou un composite de film et de tissu, de préférence où ledit composite de film et de tissu a une structure poreuse.
  12. Pansement de la revendication 10 ou procédé de la revendication 1, où ledit tissu de méduse comprend du tissu de méduse Rhopilema nomadica.
  13. Pansement de la revendication 10, comprenant en outre des agents de qualité alimentaire.
  14. Pansement de la revendication 11, où ledit film est stérilisé pendant un processus de formation de film.
  15. Pansement de la revendication 11, où ledit film a une épaisseur comprise entre 25 et 100 microns.
EP09702854.2A 2008-01-16 2009-01-18 Pansement à base de collagène colloïdal pour blessures par brûlure produit à partir de méduse Not-in-force EP2231205B1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US2138108P 2008-01-16 2008-01-16
PCT/IL2009/000071 WO2009090655A2 (fr) 2008-01-16 2009-01-18 Pansement à base de collagène colloïdal pour blessures par brûlure produit à partir de méduse

Publications (3)

Publication Number Publication Date
EP2231205A2 EP2231205A2 (fr) 2010-09-29
EP2231205A4 EP2231205A4 (fr) 2012-08-22
EP2231205B1 true EP2231205B1 (fr) 2015-04-08

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EP09702854.2A Not-in-force EP2231205B1 (fr) 2008-01-16 2009-01-18 Pansement à base de collagène colloïdal pour blessures par brûlure produit à partir de méduse

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US (2) US20100285102A1 (fr)
EP (1) EP2231205B1 (fr)
JP (1) JP5368476B2 (fr)
CN (2) CN101918047B (fr)
BR (1) BRPI0905703A2 (fr)
WO (1) WO2009090655A2 (fr)

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JP4970754B2 (ja) * 2005-08-17 2012-07-11 公立大学法人福井県立大学 クラゲ類からのコラーゲン回収方法
JP4905933B2 (ja) * 2005-08-24 2012-03-28 マルトモ株式会社 クラゲ由来のコラーゲン分解物の製造方法
JP4796914B2 (ja) * 2006-07-28 2011-10-19 公立大学法人福井県立大学 クラゲ類からのコラーゲン回収方法

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US20140193515A1 (en) 2014-07-10
WO2009090655A2 (fr) 2009-07-23
EP2231205A4 (fr) 2012-08-22
CN105709259A (zh) 2016-06-29
CN101918047B (zh) 2016-12-07
JP5368476B2 (ja) 2013-12-18
WO2009090655A3 (fr) 2010-03-11
CN101918047A (zh) 2010-12-15
US20100285102A1 (en) 2010-11-11
EP2231205A2 (fr) 2010-09-29
JP2011509734A (ja) 2011-03-31
BRPI0905703A2 (pt) 2015-07-14

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